Pseudomonas cepacia (P. multivorans) has attracted interest because of its extraordinary capacity to degrade organic compounds, its emergence as a serious cause of hospital infections, and its role as a plant pathogen. Our main objectives are (1) to exploit the catabolic versatility of P. cepacia to gain information about the integration of catabolic processes and other cellular events (2) to characterize an unusual temperate phage, CPl, associated with P. cepacia; and (3) to develop a transducing system that will permit genetic analysis of this biochemically versatile bacterium. The studies of catabolic pathways will focus on the roles of (1) glucose-6-phosphate and 6-phosphogluconate dehydrogenase isoenzymes in providing NADPH for fatty acid and reduced glutathione synthesis for assembly and maintenance of the integrity of cell membranes and (2) branched chain amino acid amino-transferase isoenzymes in formation and degradation of branched chain amino acids. The studies of phage CPl will concentrate (1) on its chemical characterization to determine if inactivation of CPl by lipid solvents is related to the presence of lipid components and define the phage DNA and proteins and (2) on its capacity to transduce P. cepacia strains. Other efforts to develop a transduction system will include screening hospital isolates and strains from the Berkeley collection for suitable temperate phage and efforts to isolate such phage from soil samples. In these experiments we will use well characterized markers related to glucose and branched chain amino acid metabolism. BIBLIOGRAPHIC REFERENCES: Lessie, T.G. and C.B. Thorne. 1976. Unusual mutations affecting branched chain amino acid biosynthesis in Bacillus licheniformis. (In Microbiology '76, in press).